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alpha Synuclein antibody - 128 211

Synucleins are involved in Parkinson's and Alzheimer's Disease
Mouse monoclonal purified IgG
Cat. No.: 128 211
Amount: 100 µg
Price: $415.00
Cat. No. 128 211 100 µg purified IgG, lyophilized. Albumin and azide were added for stabilization. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: yes
ICC: 1 : 500 gallery  
IHC: 1 : 200 gallery  
IHC-P: 1 : 500 gallery  
ELISA: yes (see remarks)
Clone 354A10D12G4
Subtype IgG1 (κ light chain)
Immunogen Synthetic peptide corresponding to AA 126 to 140 from human α-Synuclein (UniProt Id: P37840)
Epitop Epitop: AA 126 to 140 from human α-Synuclein (UniProt Id: P37840)
Reactivity Reacts with: human (P37840), rat (P37377), mouse (O55042), mammals.
Other species not tested yet.
Specificity Specific for α-synuclein, no cross-reactivity to β- and γ-synuclein.
Remarks

ELISA: This antibody is suitable as capture antibody for sandwich-ELISA with cat. no. 128 003 as detector antibody.

Data sheet 128_211.pdf

References for alpha Synuclein - 128 211

N-terminal acetylation mutants affect alpha-synuclein stability, protein levels and neuronal toxicity.
Vinueza-Gavilanes R, Íñigo-Marco I, Larrea L, Lasa M, Carte B, Santamaría E, Fernández-Irigoyen J, Bugallo R, Aragón T, Aldabe R, Arrasate M, et al.
Neurobiology of disease (2020) : 104781. 128 211 WB, ICC; tested species: human
N-terminal acetylation mutants affect alpha-synuclein stability, protein levels and neuronal toxicity.
Vinueza-Gavilanes R, Íñigo-Marco I, Larrea L, Lasa M, Carte B, Santamaría E, Fernández-Irigoyen J, Bugallo R, Aragón T, Aldabe R, Arrasate M, et al.
Neurobiology of disease (2020) : 104781. 128 211 WB, ICC; tested species: human
E46K α-synuclein pathological mutation causes cell-autonomous toxicity without altering protein turnover or aggregation.
Íñigo-Marco I, Valencia M, Larrea L, Bugallo R, Martínez-Goikoetxea M, Zuriguel I, Arrasate M
Proceedings of the National Academy of Sciences of the United States of America (2017) 11439: E8274-E8283. 128 211 ICC; tested species: rat
Multiplex imaging of human induced pluripotent stem cell-derived neurons with CO-Detection by indEXing (CODEX) technology.
Heinrich L, Zafar F, Morato Torres CA, Singh J, Khan A, Chen MY, Hempel C, Nikulina N, Mulholland J, Braubach O, Schüle B, et al.
Journal of neuroscience methods (2022) : 109653. 128 211 Codex-PC; tested species: human
Cat. No.: 128 211
Amount: 100 µg
Price: $415.00
N-terminal acetylation mutants affect alpha-synuclein stability, protein levels and neuronal toxicity.
Vinueza-Gavilanes R, Íñigo-Marco I, Larrea L, Lasa M, Carte B, Santamaría E, Fernández-Irigoyen J, Bugallo R, Aragón T, Aldabe R, Arrasate M, et al.
Neurobiology of disease (2020) : 104781. 128 211 WB, ICC; tested species: human
N-terminal acetylation mutants affect alpha-synuclein stability, protein levels and neuronal toxicity.
Vinueza-Gavilanes R, Íñigo-Marco I, Larrea L, Lasa M, Carte B, Santamaría E, Fernández-Irigoyen J, Bugallo R, Aragón T, Aldabe R, Arrasate M, et al.
Neurobiology of disease (2020) : 104781. 128 211 WB, ICC; tested species: human
E46K α-synuclein pathological mutation causes cell-autonomous toxicity without altering protein turnover or aggregation.
Íñigo-Marco I, Valencia M, Larrea L, Bugallo R, Martínez-Goikoetxea M, Zuriguel I, Arrasate M
Proceedings of the National Academy of Sciences of the United States of America (2017) 11439: E8274-E8283. 128 211 ICC; tested species: rat
Multiplex imaging of human induced pluripotent stem cell-derived neurons with CO-Detection by indEXing (CODEX) technology.
Heinrich L, Zafar F, Morato Torres CA, Singh J, Khan A, Chen MY, Hempel C, Nikulina N, Mulholland J, Braubach O, Schüle B, et al.
Journal of neuroscience methods (2022) : 109653. 128 211 Codex-PC; tested species: human
Background
Synuclein proteins are produced by three genes. They share structural resemblance to apolipoproteins, but are abundant in the neuronal cytosol and present in enriched amounts at presynaptic terminals.
Synucleins have been specifically implicated in three diseases: Alzheimer's (AD), Parkinson's (PD) and breast cancer. In AD, a peptide derived from α-synuclein forms an intrinsic component of plaque amyloid. In PD, an α-synuclein allele is genetically linked to several independent familial cases, and the protein appears to accumulate in Lewy bodies. In breast cancer, increased expression of γ-synuclein correlates with disease progression.
In songbirds, α-synuclein expression is correlated with plasticity in the developing song control system. Although the normal function of synucleins is unknown, a role in synaptic plasticity seems likely.